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Bacteriorhodopsin
Bacteriorhodopsin is an integral membrane protein used by organisms of the archaea domain, specifically halobacteria. It converts light energy to chemical energy by functioning as a proton pump that creates a proton gradient across the cell membrane. Bacteriorhodopsin subunits typically aggregate into a repeating hexagonal lattice that can cover up to half of the surface area of the cell. Retinal, a ligand found within the protein, changes its conformation upon the absorption of light. This results in a conformational change in the protein, which facilitates the proton pump.

Structure
The alpha helices shown in pink represent some of the hydrophobic elements throughout the crystallized structure of bacteriorhodopsin. The beta strands, another type of hydrophobic element in the protein, are shown in purple, while the ligands (specifically, alpha-d-glucose, retinal, and 2,10,23-trimethyl-tetracosane) embedded within the protein are displayed in yellow. Image of the 2-chain bacteriorhodopsin crystal structure crystallized from bicelles in archaeon halobacterium salinarum found at 1kme.

Contributors: Meenal Datta